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Title: ISOLATION AND CHARACTERIZATION OF THE P5 ADHESIN PROTEIN OF HAEMOPHILUS PARASUIS SEROTYPE 5

Author
item MCVICKER, JERRY - MIDLAND BIOPRODUCTS
item Tabatabai, Louisa

Submitted to: Preparative Biochemistry and Biotechnology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 1/31/2006
Publication Date: 9/1/2006
Citation: McVicker, J.K., Tabatabai, L.B. 2006. Isolation and characterization of the P5 adhesin protein of haemophilus parasuis serotype 5. Preparative Biochemistry and Biotechnology. 36(4):363-374.

Interpretive Summary: Haemophilus parasuis is a pathogen that colonizes the upper respiratory tract of young pigs. It induces a number of symptoms collectively described as Glässer’s disease. Recently, a P5-like outer membrane protein was identified in both virulent and avirulent reference strains of H. parasuis. Here we describe its purification and characterization. The purified P5 protein has an apparent molecular mass of 32,000 and its pI is 5.5. Its amino terminal sequence is homologous to that of the H. influenzae P5 protein. In contrast to the H. influenzae P5 protein, the H. parasuis P5 protein does not react with the carcinoembryonic antigen (CEA) an epithelial cell adhesion molecule.

Technical Abstract: Haemophilus parasuis is a Gram-negative respiratory pathogen of young pigs that colonizes the upper respiratory tract and produces a number of symptoms collectively described as Glässer’s disease. Recently, an H. parasuis P5-like outer membrane adhesin protein homologous to H. influenzae P5 was identified. The P5 adhesin was partially purified by anion exchange and size-exclusion chromatography. Final purification for functional studies was performed by elution of the protein from a polyacrylamide gel. Identification of the protein as a P5 adhesin homolog of H. influenzae was confirmed by N-terminal sequencing. The P5 protein had a molecular mass of 32,000 and a pI of 5.5. Unlike the H. influenzae P5 adhesin, the H. parasuis P5 protein did not bind carcinoembryonic antigen (CEA).